Serrano Irene, Campos Laura, Rivas Susana
LIPM, Université de Toulouse, INRA, CNRS, Castanet-Tolosan, France.
Front Plant Sci. 2018 Feb 8;9:139. doi: 10.3389/fpls.2018.00139. eCollection 2018.
Ubiquitination, the reversible protein conjugation with ubiquitin (Ub), is a post-translational modification that enables rapid and specific cellular responses to stimuli without requirement of protein synthesis. Although ubiquitination also displays non-proteolytic functions, it often acts as a signal for selective protein degradation through the ubiquitin-proteasome system (UPS). In plants, it has become increasingly apparent that the UPS is a central regulator of many key cellular and physiological processes, including responses to biotic and abiotic stresses. In the nucleus, protein regulation the UPS orchestrates gene expression, genome maintenance, and signal transduction. Here, we focus on E3 Ub-ligase proteins as major components of the ubiquitination cascade that confer specificity of substrate recognition. We provide an overview on how they contribute to nuclear proteome plasticity during plant responses to environmental stress signals.
泛素化是一种蛋白质与泛素(Ub)的可逆结合,是一种翻译后修饰,能够使细胞对刺激做出快速而特异的反应,而无需蛋白质合成。尽管泛素化也具有非蛋白水解功能,但它通常作为一种信号,通过泛素-蛋白酶体系统(UPS)介导选择性蛋白质降解。在植物中,越来越明显的是,UPS是许多关键细胞和生理过程的核心调节因子,包括对生物和非生物胁迫的反应。在细胞核中,UPS协调蛋白质调控、基因表达、基因组维持和信号转导。在这里,我们重点关注E3泛素连接酶蛋白,它们是泛素化级联反应的主要组成部分,赋予底物识别特异性。我们概述了它们如何在植物对环境胁迫信号的反应过程中促进核蛋白质组的可塑性。